Fast kinetics of nucleotide binding to Clostridium perfringens family II pyrophosphatase containing CBS and DRTGG domains

Biochemistry. Biokhimii︠a︡
Joonas JämsenReijo Lahti

Abstract

We earlier described CBS-pyrophosphatase of Moorella thermoacetica (mtCBS-PPase) as a novel phosphohydrolase that acquired a pair of nucleotide-binding CBS domains during evolution, thus endowing the protein with the capacity to be allosterically regulated by adenine nucleotides (Jämsen, J., Tuominen, H., Salminen, A., Belogurov, G. A., Magretova, N. N., Baykov, A. A., and Lahti, R. (2007) Biochem. J., 408, 327-333). We herein describe a more evolved type of CBS-pyrophosphatase from Clostridium perfringens (cpCBS-PPase) that additionally contains a DRTGG domain between the two CBS domains in the regulatory part. cpCBS-PPase retained the ability of mtCBS-PPase to be inhibited by micromolar concentrations of AMP and ADP and activated by ATP and was additionally activated by diadenosine polyphosphates (AP(n)A) with n > 2. Stopped-flow measurements using a fluorescent nucleotide analog, 2'(3')-O-(N-methylanthranoyl)-AMP, revealed that cpCBS-PPase interconverts through two different conformations with transit times on the millisecond scale upon nucleotide binding. The results suggest that the presence of the DRTGG domain affords greater flexibility to the regulatory part, allowing it to more rapidly undergo conformational changes in...Continue Reading

References

Jul 1, 1992·Trends in Biochemical Sciences·B S CoopermanR Lahti
Jan 1, 1994·Advances in Microbial Physiology·P Plateau, S Blanquet
Jun 5, 1998·Trends in Biochemical Sciences·A Nishimura
Aug 17, 1999·Progress in Molecular and Subcellular Biology·A A BaykovR Lahti
Jan 15, 2004·The Journal of Clinical Investigation·John W ScottD Grahame Hardie
Nov 9, 2005·American Journal of Physiology. Cell Physiology·Sofie Ignoul, Jan Eggermont

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